Identification and Expression Patterns of fvexpl1, an Expansin-Like Protein-Encoding Gene, Suggest an Auxiliary Role in the Stipe Morphogenesis of Flammulina velutipes
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Expansins are cell wall proteins that mediate cell wall loosening and promote specific tissue and organ morphogenesis in plants and in some microorganisms. Unlike plant expansins, the biological functions of fungal expansin-like proteins have rarely been discussed. In the present study, an expansin-like protein-encoding fvexpl1 gene, was identified from Flammulina velutipes by using local BLAST. It consisted of five exons with a total length of 822 bp. The deduced protein FVEXPL1 contained 274 amino acids with a predicted molecular mass and isoelectric point of 28,589 Da and pH 4.93, respectively. The first 19 amino acids from the N terminal are the signal peptide. Phylogenetic analysis and multiple protein alignment indicated FVEXPL1 was an expansin-like protein. The expression level of fvexpl1 gene in the stipe was significantly higher than that in the mycelia, primordia, and cap. However, the expression level of fvexpl1 gene was significantly higher in the fast elongation region of the stipe as compared with the slow elongation region. Expression analysis indicated that fvexpl1 gene might have an auxiliary role in the stipe morphogenesis of F. velutipes.
Abstract
Expansins are cell wall proteins that mediate cell wall loosening and promote specific tissue and organ morphogenesis in plants and in some microorganisms. Unlike plant expansins, the biological functions of fungal expansin-like proteins have rarely been discussed. In the present study, an expansin-like protein-encoding fvexpl1 gene, was identified from Flammulina velutipes by using local BLAST. It consisted of five exons with a total length of 822 bp. The deduced protein FVEXPL1 contained 274 amino acids with a predicted molecular mass and isoelectric point of 28,589 Da and pH 4.93, respectively. The first 19 amino acids from the N terminal are the signal peptide. Phylogenetic analysis and multiple protein alignment indicated FVEXPL1 was an expansin-like protein. The expression level of fvexpl1 gene in the stipe was significantly higher than that in the mycelia, primordia, and cap. However, the expression level of fvexpl1 gene was significantly higher in the fast elongation region of the stipe as compared with the slow elongation region. Expression analysis indicated that fvexpl1 gene might have an auxiliary role in the stipe morphogenesis of F. velutipes.
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